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 Blood, 30 April 2009, Vol. 113, No. 18, pp. 4425-4430.
Prepublished online as a Blood First Edition Paper on December 15, 2008; DOI 10.1182/blood-2008-09-178178.

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THROMBOSIS AND HEMOSTASIS

Fibrinogen variant BβD432A has normal polymerization but does not bind knob "B"

Sheryl R. Bowley1, and Susan T. Lord1,2

1 Department of Chemistry and 2 Department of Pathology and Laboratory Medicine, University of North Carolina, Chapel Hill

Fibrinogen residue Bβ432Asp is part of hole "b" that interacts with knob "B," whose sequence starts with Gly-His-Arg-Pro-amide (GHRP). Because previous studies showed BβD432A has normal polymerization, we hypothesized that Bβ432Asp is not critical for knob "B" binding and that new knob-hole interactions would compensate for the loss of this Asp residue. To test this hypothesis, we solved the crystal structure of fragment D from BβD432A. Surprisingly, the structure (rfD-BβD432A+GH) showed the peptide GHRP was not bound to hole "b." We then re-evaluated the polymerization of this variant by examining clot turbidity, clot structure, and the rate of FXIIIa cross-linking. The turbidity and the rate of {gamma}-{gamma} dimer formation for BβD432A were indistinguishable compared with normal fibrinogen. Scanning electron microscopy showed no significant differences between the clots of BβD432A and normal, but the thrombin-derived clots had thicker fibers than clots obtained from batroxobin, suggesting that cleavage of FpB is more important than "B:b" interactions. We conclude that hole "b" and "B:b" knob-hole binding per se have no influence on fibrin polymerization.


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